Striatin, a calmodulin‐dependent scaffolding protein, directly binds caveolin‐1

Gaillard, Stéphane; Bartoli, Marc; Castets, Francis; Monneron, Ariane

doi:10.1016/s0014-5793(01)03020-4

Cited by 65 publications

(76 citation statements)

References 29 publications

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“…It is important to consider the subcellular localization of the PRO11 WD40 protein because mammalian homologues, such as striatin, SG2NA, and zinedin, are neuronal proteins that are strictly expressed in the somatodendritic compartments. These are found in the cytosol and are also associated with membranes (11,16,38).…”

Section: Resultsmentioning

confidence: 99%

“…In addition, they are endowed with diverse protein-protein association modules, for instance, a caveolin-binding motif, a coiled-coil structure, a Ca 2ϩ -calmodulin-binding domain, and multiple WD40 repeats homologous to WD40 repeats in the beta subunit of trimeric G-proteins. Due to these domains, proteins of the striatin family are engaged in multiple protein associations and are thought to act as scaffolds as well as signaling proteins (5,10,11,16).…”

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confidence: 99%

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A WD40 Repeat Protein Regulates Fungal Cell Differentiation and Can Be Replaced Functionally by the Mammalian Homologue Striatin

2004

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Fruiting body development in fungi is a complex cellular differentiation process that is controlled by more than 100 developmental genes. Mutants of the filamentous fungus Sordaria macrospora showing defects in fruiting body formation are pertinent sources for the identification of components of this multicellular differentiation process. Here we show that the sterile mutant pro11 carries a defect in the pro11 gene encoding a multimodular WD40 repeat protein. Complementation analysis indicates that the wild-type gene or Cterminally truncated versions of the wild-type protein are able to restore the fertile phenotype in mutant pro11. PRO11 shows significant homology to several vertebrate WD40 proteins, such as striatin and zinedin, which seem to be involved in Ca 2؉ -dependent signaling in cells of the central nervous system and are supposed to function as scaffolding proteins linking signaling and eukaryotic endocytosis. Cloning of a mouse cDNA encoding striatin allowed functional substitution of the wild-type protein with restoration of fertility in mutant pro11. Our data strongly suggest that an evolutionarily conserved cellular process controlling eukaryotic cell differentiation may regulate fruiting body formation.

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Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

A WD40 Repeat Protein Regulates Fungal Cell Differentiation and Can Be Replaced Functionally by the Mammalian Homologue Striatin

2004

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“…Mammalian cells contain a two related proteins, striatin and SG2NA, that also interact with the PP2A core dimer [45]. These proteins have been linked to regulation of the cytoskeleton [46], lipid raft formation [47], and non-genomic actions of the estrogen receptor [48]. BLAST searches of the Drosophila genome identified a gene (Cka) encoding a transcript with 36% identity to human striatin and SG2NA.…”

Section: Discussionmentioning

confidence: 99%

Functional analysis of the PP2A subfamily of protein phosphatases in regulating Drosophila S6 kinase

Bielinski¹,

Mumby²

2007

Experimental Cell Research

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Phosphorylation and activation of ribosomal S6 protein kinase is an important link in the regulation of cell size by the target of rapamycin (TOR) protein kinase. A combination of selective inhibition and RNA interference were used to test the roles of members of the PP2A subfamily of protein phosphatases in dephosphorylation of Drosophila S6 kinase (dS6K). Treatment of Drosophila Schneider 2 cells with calyculin A, a selective inhibitor of PP2A-like phosphatases, resulted in a 7-fold increase in the basal level of dS6K phosphorylation at the TOR phosphorylation site (Thr398) and blocked dephosphorylation following inactivation of TOR by amino acid starvation or rapamycin treatment. Knockdown of the PP2A catalytic subunit increased basal dS6K phosphorylation and inhibited dephosphorylation induced by amino acid withdrawal. In contrast, depletion of the catalytic subunits of the other two members of the subfamily did not enhance dS6K phosphorylation. Knockdown of PP4 caused a 20% decrease in dS6K phosphorylation and knockdown of PP6 had no effect. Knockdown of the Drosophila B56-2 subunit resulted in enhanced dephosphorylation of dS6K following removal of amino acids. In contrast, knockdown of the homologs of the other PP2A regulatory subunits had no effects. Knockdown of the Drosophila homolog of the PP2A/PP4/PP6 interaction protein α4/Tap42 did not affect S6K phosphorylation, but did induce apoptosis. These results indicate that PP2A, but not other members of this subfamily, is likely to be a major S6K phosphatase in intact cells and is consistent with an important role for this phosphatase in the TOR pathway.

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“…Striatin contains the caveolin-binding consensus motif: LHFIQHEWARF, and binds directly caveolin-1 (Gaillard et al, 2001). -Coiled-coil domain: Coiled-coil domains allow homoand hetero-oligomerization.…”

Section: Proteinmentioning

confidence: 99%

“…-Relation with caveolins: striatin directly binds caveolin-1 (Gaillard et al, 2001), a palmitoylated protein involved in caveolae and lipid rafts. Caveolins are scaffolding proteins, the main components of caveolae.…”

Section: Functionmentioning

confidence: 99%

STRN (striatin, calmodulin binding protein)

Huret¹

2011

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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Striatin, a calmodulin‐dependent scaffolding protein, directly binds caveolin‐1

Cited by 65 publications

References 29 publications

A WD40 Repeat Protein Regulates Fungal Cell Differentiation and Can Be Replaced Functionally by the Mammalian Homologue Striatin

A WD40 Repeat Protein Regulates Fungal Cell Differentiation and Can Be Replaced Functionally by the Mammalian Homologue Striatin

Functional analysis of the PP2A subfamily of protein phosphatases in regulating Drosophila S6 kinase

STRN (striatin, calmodulin binding protein)

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